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Molecular bases of thermophily in hyperthermophiles
I reflect on some of our studies on the hyperthermophilic archaeon, Thermococcus kodakarensis KOD1 and its enzymes. The strain can grow at temperatures up to 100 ℃, and also represents one of the simplest forms of life. As expected, all enzymes, DNA, RNA, cytoplasmic membrane, and cytoplasmic solute...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Japan Academy
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3309922/ https://www.ncbi.nlm.nih.gov/pubmed/22075760 http://dx.doi.org/10.2183/pjab.87.587 |
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author | IMANAKA, Tadayuki |
author_facet | IMANAKA, Tadayuki |
author_sort | IMANAKA, Tadayuki |
collection | PubMed |
description | I reflect on some of our studies on the hyperthermophilic archaeon, Thermococcus kodakarensis KOD1 and its enzymes. The strain can grow at temperatures up to 100 ℃, and also represents one of the simplest forms of life. As expected, all enzymes, DNA, RNA, cytoplasmic membrane, and cytoplasmic solute displayed remarkable thermostability, and we have determined some of the basic principles that govern this feature. To our delight, many of the enzymes exhibited unique biochemical properties and novel structures not found in mesophilic proteins. Here, I will focus on some enzymes whose three-dimensional structures are characteristic of thermostable enzymes. I will also add some examples on the stabilization of DNA, RNA, cytoplasmic membrane, and cytoplasmic solute. |
format | Online Article Text |
id | pubmed-3309922 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Japan Academy |
record_format | MEDLINE/PubMed |
spelling | pubmed-33099222012-04-20 Molecular bases of thermophily in hyperthermophiles IMANAKA, Tadayuki Proc Jpn Acad Ser B Phys Biol Sci Review I reflect on some of our studies on the hyperthermophilic archaeon, Thermococcus kodakarensis KOD1 and its enzymes. The strain can grow at temperatures up to 100 ℃, and also represents one of the simplest forms of life. As expected, all enzymes, DNA, RNA, cytoplasmic membrane, and cytoplasmic solute displayed remarkable thermostability, and we have determined some of the basic principles that govern this feature. To our delight, many of the enzymes exhibited unique biochemical properties and novel structures not found in mesophilic proteins. Here, I will focus on some enzymes whose three-dimensional structures are characteristic of thermostable enzymes. I will also add some examples on the stabilization of DNA, RNA, cytoplasmic membrane, and cytoplasmic solute. The Japan Academy 2011-11-11 /pmc/articles/PMC3309922/ /pubmed/22075760 http://dx.doi.org/10.2183/pjab.87.587 Text en © 2011 The Japan Academy This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review IMANAKA, Tadayuki Molecular bases of thermophily in hyperthermophiles |
title | Molecular bases of thermophily in hyperthermophiles |
title_full | Molecular bases of thermophily in hyperthermophiles |
title_fullStr | Molecular bases of thermophily in hyperthermophiles |
title_full_unstemmed | Molecular bases of thermophily in hyperthermophiles |
title_short | Molecular bases of thermophily in hyperthermophiles |
title_sort | molecular bases of thermophily in hyperthermophiles |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3309922/ https://www.ncbi.nlm.nih.gov/pubmed/22075760 http://dx.doi.org/10.2183/pjab.87.587 |
work_keys_str_mv | AT imanakatadayuki molecularbasesofthermophilyinhyperthermophiles |